1dfl
From Proteopedia
(New page: 200px<br /><applet load="1dfl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dfl, resolution 4.20Å" /> '''SCALLOP MYOSIN S1 CO...) |
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| - | [[Image:1dfl.jpg|left|200px]]<br /><applet load="1dfl" size=" | + | [[Image:1dfl.jpg|left|200px]]<br /><applet load="1dfl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dfl, resolution 4.20Å" /> | caption="1dfl, resolution 4.20Å" /> | ||
'''SCALLOP MYOSIN S1 COMPLEXED WITH MGADP:VANADATE-TRANSITION STATE'''<br /> | '''SCALLOP MYOSIN S1 COMPLEXED WITH MGADP:VANADATE-TRANSITION STATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the structure of the intact scallop myosin head, containing both the motor domain and the lever arm, in the nucleotide-free | + | We have determined the structure of the intact scallop myosin head, containing both the motor domain and the lever arm, in the nucleotide-free state and in the presence of MgADP.V04, corresponding to the transition state. These two new structures, together with the previously determined structure of scallop S1 complexed with MgADP (which we interpret as a detached ATP state), reveal three conformations of an intact S1 obtained from a single isoform. These studies, together with new crystallization results, show how the conformation of the motor depends on the nucleotide content of the active site. The resolution of the two new structures ( approximately 4 A) is sufficient to establish the relative positions of the subdomains and the overall conformation of the joints within the motor domain as well as the position of the lever arm. Comparison of available crystal structures from different myosin isoforms and truncated constructs in either the nucleotide-free or transition states indicates that the major features within the motor domain are relatively invariant in both these states. In contrast, the position of the lever arm varies significantly between different isoforms. These results indicate that the heavy-chain helix is pliant at the junction between the converter and the lever arm and that factors other than the precise position of the converter can influence the position of the lever arm. It is possible that this pliant junction in the myosin head contributes to the compliance known to be present in the crossbridge. |
==About this Structure== | ==About this Structure== | ||
| - | 1DFL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians] with CA, MG, VO4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1DFL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=VO4:'>VO4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cohen, C.]] | [[Category: Cohen, C.]] | ||
[[Category: Houdusse, A.]] | [[Category: Houdusse, A.]] | ||
| - | [[Category: Szent-Gyorgyi, A | + | [[Category: Szent-Gyorgyi, A G.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: myosin motor]] | [[Category: myosin motor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:09 2008'' |
Revision as of 10:16, 21 February 2008
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SCALLOP MYOSIN S1 COMPLEXED WITH MGADP:VANADATE-TRANSITION STATE
Overview
We have determined the structure of the intact scallop myosin head, containing both the motor domain and the lever arm, in the nucleotide-free state and in the presence of MgADP.V04, corresponding to the transition state. These two new structures, together with the previously determined structure of scallop S1 complexed with MgADP (which we interpret as a detached ATP state), reveal three conformations of an intact S1 obtained from a single isoform. These studies, together with new crystallization results, show how the conformation of the motor depends on the nucleotide content of the active site. The resolution of the two new structures ( approximately 4 A) is sufficient to establish the relative positions of the subdomains and the overall conformation of the joints within the motor domain as well as the position of the lever arm. Comparison of available crystal structures from different myosin isoforms and truncated constructs in either the nucleotide-free or transition states indicates that the major features within the motor domain are relatively invariant in both these states. In contrast, the position of the lever arm varies significantly between different isoforms. These results indicate that the heavy-chain helix is pliant at the junction between the converter and the lever arm and that factors other than the precise position of the converter can influence the position of the lever arm. It is possible that this pliant junction in the myosin head contributes to the compliance known to be present in the crossbridge.
About this Structure
1DFL is a Protein complex structure of sequences from Argopecten irradians with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Three conformational states of scallop myosin S1., Houdusse A, Szent-Gyorgyi AG, Cohen C, Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11238-43. PMID:11016966
Page seeded by OCA on Thu Feb 21 12:16:09 2008
